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Molecular basis of the flavin‐based electron‐bifurcating caffeyl‐CoA reductase reaction

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Demmer,  Julius K.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kayastha,  Kanwal
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Demmer,  Ulrike
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Demmer, J. K., Bertsch, J., Öppinger, C., Wohlers, H., Kayastha, K., Demmer, U., et al. (2018). Molecular basis of the flavin‐based electron‐bifurcating caffeyl‐CoA reductase reaction. FEBS Letters, 592(3), 332-342. doi:10.1002/1873-3468.12971.


Cite as: http://hdl.handle.net/21.11116/0000-0002-6692-6
Abstract
Flavin‐based electron bifurcation (FBEB) is a recently discovered mode of energy coupling in anaerobic microorganisms. The electron‐bifurcating caffeyl‐CoA reductase (CarCDE) catalyzes the reduction of caffeyl‐CoA and ferredoxin by oxidizing NADH. The 3.5 Å structure of the heterododecameric Car(CDE)4 complex of Acetobacterium woodii, presented here, reveals compared to other electron‐transferring flavoprotein/acyl dehydrogenase family members an additional ferredoxin‐like domain with two [4Fe–4S] clusters N‐terminally fused to CarE. It might serve, in vivo, as specific adaptor for the physiological electron acceptor. Kinetic analysis of a CarCDE(∆Fd) complex indicates the bypassing of the ferredoxin‐like domain by artificial electron acceptors. Site‐directed mutagenesis studies substantiated the crucial role of the C‐terminal arm of CarD and of ArgE203, hydrogen‐bonded to the bifurcating FAD, for FBEB.